Pervasive, conserved secondary structure in highly charged protein regions
Fig 5
Highly charged regions are evolutionarily conserved.
a The distribution of gap frequencies (left) and average position-wise entropy (right) summarizing multiple sequence alignments (MSAs) of the highly charged regions (purple), randomly drawn regions from the rest of the proteins that contain them (black), and IDRs from DisProt (gray). b Summary of the variance (in log odds space) of usage of categories of amino acids for all proteomes in the AYbRAH database. c FCR values, averaged across AYbRAH alignments, for the highly charged regions identified in the S. cerevisiae proteome and length-matched randomly-drawn regions and their associated AYbRAH MSA. d The average compositional conservation of regions enriched for all sets of four amino acids with the same total frequency as the charged amino acids, plotted as a CDF. Higher values indicate less drift, and lower values indicate more drift (regression to the proteome average).